ID   ALO_YEAST               Reviewed;         526 AA.
AC   P54783; O42618;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 80.
DE   RecName: Full=D-arabinono-1,4-lactone oxidase;
DE            Short=ALO;
DE            EC=1.1.3.37;
DE   AltName: Full=L-galactono-gamma-lactone oxidase;
GN   Name=ALO1; OrderedLocusNames=YML086C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 86-105 AND
RP   349-363.
RC   STRAIN=ATCC 44774 / DBY747;
RX   MEDLINE=99140446; PubMed=10094636;
RX   DOI=10.1046/j.1365-2958.1998.01133.x;
RA   Huh W.-K., Lee B.-H., Kim S.-T., Kim Y.-R., Rhie G.-E., Baek Y.-W.,
RA   Hwang C.-S., Lee J.-S., Kang S.-O.;
RT   "D-erythroascorbic acid is an important antioxidant molecule in
RT   Saccharomyces cerevisiae.";
RL   Mol. Microbiol. 30:895-903(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Nishikimi M., Ohata Y., Ishikawa T.;
RT   "Identification of the yeast genomic sequence encoding L-galactono-
RT   gamma-lactone oxidase.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313268; PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
RA   Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
RA   Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   XIII.";
RL   Nature 387:90-93(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Can oxidize L-gulono-1,4-lactone as well as D-arabinono-
CC       1,4-lactone and L-galactono-1,4-lactone.
CC   -!- CATALYTIC ACTIVITY: D-arabinono-1,4-lactone + O(2) = dehydro-D-
CC       arabinono-1,4-lactone + H(2)O(2).
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Cofactor biosynthesis; D-erythroascorbic acid
CC       biosynthesis; D-erythro-ascorbic acid from D-arabinose: step 2/2.
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-2519, EBI-2519;
CC       P38756:-; NbExp=1; IntAct=EBI-2519, EBI-24431;
CC       P38845:-; NbExp=1; IntAct=EBI-2519, EBI-24770;
CC       P31787:ACB1; NbExp=1; IntAct=EBI-2519, EBI-2060;
CC       P38009:ADE17; NbExp=1; IntAct=EBI-2519, EBI-14223;
CC       P11076:ARF1; NbExp=1; IntAct=EBI-2519, EBI-2816;
CC       P53090:ARO8; NbExp=1; IntAct=EBI-2519, EBI-2042933;
CC       P43497:CWP2; NbExp=1; IntAct=EBI-2519, EBI-2044078;
CC       P32582:CYS4; NbExp=1; IntAct=EBI-2519, EBI-4167;
CC       Q12091:DAP1; NbExp=1; IntAct=EBI-2519, EBI-5554;
CC       P20449:DBP5; NbExp=1; IntAct=EBI-2519, EBI-5617;
CC       P54861:DNM1; NbExp=1; IntAct=EBI-2519, EBI-6002;
CC       P38295:EHT1; NbExp=1; IntAct=EBI-2519, EBI-20890;
CC       P39002:FAA3; NbExp=1; IntAct=EBI-2519, EBI-10089;
CC       P18411:FUN14; NbExp=1; IntAct=EBI-2519, EBI-20609;
CC       P32288:GLN1; NbExp=1; IntAct=EBI-2519, EBI-7665;
CC       P40582:GTT1; NbExp=1; IntAct=EBI-2519, EBI-7941;
CC       P22943:HSP12; NbExp=1; IntAct=EBI-2519, EBI-8548;
CC       Q6Q5K6:HUG1; NbExp=1; IntAct=EBI-2519, EBI-392766;
CC       P40581:HYR1; NbExp=1; IntAct=EBI-2519, EBI-7869;
CC       P47031:IML2; NbExp=1; IntAct=EBI-2519, EBI-25966;
CC       P11986:INO1; NbExp=1; IntAct=EBI-2519, EBI-9257;
CC       P00817:IPP1; NbExp=1; IntAct=EBI-2519, EBI-9338;
CC       P35844:KES1; NbExp=1; IntAct=EBI-2519, EBI-9648;
CC       Q12230:LSP1; NbExp=1; IntAct=EBI-2519, EBI-34978;
CC       P36060:MCR1; NbExp=1; IntAct=EBI-2519, EBI-10565;
CC       P28737:MSP1; NbExp=1; IntAct=EBI-2519, EBI-11435;
CC       Q03558:OYE2; NbExp=1; IntAct=EBI-2519, EBI-12729;
CC       P10963:PCK1; NbExp=1; IntAct=EBI-2519, EBI-13770;
CC       P37012:PGM2; NbExp=1; IntAct=EBI-2519, EBI-13296;
CC       P87284:PMP3; NbExp=1; IntAct=EBI-2519, EBI-13555;
CC       P22289:QCR9; NbExp=1; IntAct=EBI-2519, EBI-19947;
CC       Q00578:RAD25; NbExp=1; IntAct=EBI-2519, EBI-14683;
CC       P21524:RNR1; NbExp=1; IntAct=EBI-2519, EBI-15234;
CC       P09938:RNR2; NbExp=1; IntAct=EBI-2519, EBI-15240;
CC       P39954:SAH1; NbExp=1; IntAct=EBI-2519, EBI-16451;
CC       P14693:SAM35; NbExp=1; IntAct=EBI-2519, EBI-24602;
CC       P07560:SEC4; NbExp=1; IntAct=EBI-2519, EBI-16858;
CC       P25294:SIS1; NbExp=1; IntAct=EBI-2519, EBI-17244;
CC       P33328:SNC2; NbExp=1; IntAct=EBI-2519, EBI-17512;
CC       P39929:SNF7; NbExp=1; IntAct=EBI-2519, EBI-17554;
CC       P35180:TOM20; NbExp=1; IntAct=EBI-2519, EBI-12522;
CC       P07213:TOM70; NbExp=1; IntAct=EBI-2519, EBI-12551;
CC       P38342:TSC10; NbExp=1; IntAct=EBI-2519, EBI-21124;
CC       Q08926:UIP4; NbExp=1; IntAct=EBI-2519, EBI-2044051;
CC       P28274:URA7; NbExp=1; IntAct=EBI-2519, EBI-20128;
CC       P07806-1:VAS1; NbExp=1; IntAct=EBI-2519, EBI-1009942;
CC       P0C268:YBL039W-B; NbExp=1; IntAct=EBI-2519, EBI-2044092;
CC       Q3E6R5:YDR381C-A; NbExp=1; IntAct=EBI-2519, EBI-2044020;
CC       P53206:YGR012W; NbExp=1; IntAct=EBI-2519, EBI-2044073;
CC       P01123:YPT1; NbExp=1; IntAct=EBI-2519, EBI-29496;
CC       P38555:YPT31; NbExp=1; IntAct=EBI-2519, EBI-29379;
CC       P51996:YPT32; NbExp=1; IntAct=EBI-2519, EBI-29384;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane. Note=Membrane-
CC       embedded.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: Present with 6190 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked
CC       oxidoreductase family.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
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DR   EMBL; U40390; AAC98538.1; -; Genomic_DNA.
DR   EMBL; AB009401; BAA23804.1; -; Genomic_DNA.
DR   EMBL; Z46660; CAA86652.1; -; Genomic_DNA.
DR   EMBL; AY693120; AAT93139.1; -; Genomic_DNA.
DR   PIR; S49641; S49641.
DR   RefSeq; NP_013624.1; -.
DR   IntAct; P54783; 64.
DR   PeptideAtlas; P54783; -.
DR   Ensembl; YML086C; Saccharomyces cerevisiae.
DR   GeneID; 854888; -.
DR   GenomeReviews; Z71257_GR; YML086C.
DR   KEGG; sce:YML086C; -.
DR   NMPDR; fig|4932.3.peg.4661; -.
DR   CYGD; YML086c; -.
DR   SGD; S000004551; ALO1.
DR   HOGENOM; P54783; -.
DR   OMA; P54783; DCLFSQF.
DR   BRENDA; 1.1.3.37; 250.
DR   NextBio; 977843; -.
DR   GermOnline; YML086C; Saccharomyces cerevisiae.
DR   GO; GO:0031307; C:integral to mitochondrial outer membrane; IDA:SGD.
DR   GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IDA:SGD.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0070485; P:dehydro-D-arabinono-1,4-lactone biosyntheti...; IMP:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:SGD.
DR   InterPro; IPR007173; ALO.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR010031; FAD_lactone_oxidase.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   Pfam; PF04030; ALO; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   TIGRFAMs; TIGR01678; FAD_lactone_ox; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; FAD; Flavoprotein;
KW   Membrane; Mitochondrion; Oxidoreductase.
FT   CHAIN         1    526       D-arabinono-1,4-lactone oxidase.
FT                                /FTId=PRO_0000128171.
FT   DOMAIN       19    193       FAD-binding PCMH-type.
FT   MOD_RES      56     56       Tele-8alpha-FAD histidine (By
FT                                similarity).
FT   CONFLICT    417    417       A -> P (in Ref. 2; BAA23804).
SQ   SEQUENCE   526 AA;  59494 MW;  942177A74A738EC8 CRC64;
     MSTIPFRKNY VFKNWAGIYS AKPERYFQPS SIDEVVELVK SARLAEKSLV TVGSGHSPSN
     MCVTDEWLVN LDRLDKVQKF VEYPELHYAD VTVDAGMRLY QLNEFLGAKG YSIQNLGSIS
     EQSVAGIIST GSHGSSPYHG LISSQYVNLT IVNGKGELKF LDAENDPEVF KAALLSVGKI
     GIIVSATIRV VPGFNIKSTQ EVITFENLLK QWDTLWTSSE FIRVWWYPYT RKCVLWRGNK
     TTDAQNGPAK SWWGTKLGRF FYETLLWIST KIYAPLTPFV EKFVFNRQYG KLEKSSTGDV
     NVTDSISGFN MDCLFSQFVD EWGCPMDNGL EVLRSLDHSI AQAAINKEFY VHVPMEVRCS
     NTTLPSEPLD TSKRTNTSPG PVYGNVCRPF LDNTPSHCRF APLENVTNSQ LTLYINATIY
     RPFGCNTPIH KWFTLFENTM MVAGGKPHWA KNFLGSTTLA AGPVKKDTDY DDFEMRGMAL
     KVEEWYGEDL KKFRKIRKEQ DPDNVFLANK QWAIINGIID PSELSD
//